› 4uws

X-ray diffraction
1.66Å resolution

VIM-26-PEG. Leu224 in VIM-26 from Klebsiella pneumoniae has implications for drug binding.

Released:
DOI: 10.2210/pdb4uws/pdb
PDB entry 4uws coloured by chain, front view.
PDB entry 4uws coloured by chain, side view.
PDB entry 4uws coloured by chain, top view.
Source organism: Klebsiella pneumoniae
Primary publication:
Structural and biochemical characterization of VIM-26 shows that Leu224 has implications for the substrate specificity of VIM metallo-β-lactamases.
Leiros HK, Edvardsen KS, Bjerga GE, Samuelsen Ø
FEBS J 282 1031-42 (2015)
PMID: 25601024

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-122963 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Metallo-beta-lactamase type 2 Chain: B
Molecule details ›
Chain: B
Length: 266 amino acids
Theoretical weight: 28.07 KDa
Source organism: Klebsiella pneumoniae
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: E5BDC6 (Residues: 1-266; Coverage: 100%)
Gene name: blaVIM-26
Sequence domains: Metallo-beta-lactamase superfamily
Structure domains: Ribonuclease Z/Hydroxyacylglutathione hydrolase-like

Ligands and Environments

4 bound ligands:
Ligand SO4 1 x SO4
Ligand ZN 2 x ZN
Ligand PEG 1 x PEG
Ligand EDO 1 x EDO
1 modified residue:
Ligand OCS 1 x OCS

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.1
Spacegroup: P21
Unit cell:
a: 39.759Å b: 68.172Å c: 40.406Å
α: 90° β: 92.56° γ: 90°
R-values:
R R work R free
0.158 0.156 0.2
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 review citations

Metallo-β-lactamases in the Age of Multidrug Resistance: From Structure and Mechanism to Evolution, Dissemination, and Inhibitor Design.
Bahr et al. (2021)
1 more